|Related Categories||Cell Biology, Cytochrome c Control Proteins, Cytochromes, Electron Transport and Cellular Respiration, Gel Filtration Chromatography,|
|mol wt||mol wt ~12,400|
|packaging||vial of ≥10 mg|
|suitability||suitable for GFC marker|
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Cytochrome c is primarily known as an electron-carrying mitochondrial protein. The transition of cytochrome c between the ferrous and ferric states within the cell makes it an efficient biological electron-transporter and it plays a vital role in cellular oxidations in both plants and animals. It is generally regarded as a universal catalyst of respiration, forming an essential electron-bridge between the respirable substrates and oxygen
Cytochrome c is primarily known as an electron-carrying mitochondrial protein and is generally regarded as a universal catalyst of respiration. Cytochrome c can be used as a gel filtration molecular weight marker in gel filtration chromatography and protein chromatography and can be used to study cytochrome c control proteins, electron transport and cellular respiration.
The specific sites and extent of oxidation in horse cytochrome c treated with H2O2 and UV were characterized. It was suggested that the state of these sites could be used as a biomarker for the oxidative environment in a cell.
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≥95% based on Mol. Wt. 12,384 basis
BioUltra, ≥99% (SDS-PAGE)
Certificate of Analysis
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The effects of ATP and sodium chloride on the cytochrome c-cardiolipin interaction: the contrasting behavior of the horse heart and yeast proteins. Sinibaldi, F., et al. J. Inorg. Biochem. 105, 1365-1372, (2011)
[Electrochemical sensor systems based on one dimensional (1D) nanostructures for analysis of bioaffinity interactions]. Shumiantseva VV, Bulko TV, suprun EV, et al. Biomed. Khim. 59(2), 209-18, (2013)
Propofol protects against nitrosative stress-induced apoptotic insults to cerebrovascular endothelial cells via an intrinsic mitochondrial mechanism. Chen RM, Tai YT, Chen TG, et al. Surgery 154(1), 58-68, (2013)
Recognition and binding of apocytochrome c to P. aeruginosa CcmI, a component of cytochrome c maturation machinery. Di Silvio E, Di Matteo A, Malatesta F, et al. Biochim. Biophys. Acta 1834(8), 1554-61, (2013)
Crotonaldehyde induces apoptosis in alveolar macrophages through intracellular calcium, mitochondria and p53 signaling pathways. Yang BC, Pan XJ, Yang ZH, et al. J. Toxicol. Sci. 38(2), 225-35, (2013)
Expression, purification, characterization, and solution nuclear magnetic resonance study of highly deuterated yeast cytochrome C peroxidase with enhanced solubility. Volkov AN, Wohlkonig A, Soror SH, et al. Biochemistry 52(13), 2165-75, (2013)
Modulatory effects of phytoestrogens on the expression of Fas ligand and the release of cytochrome C in normal and cancerous endometrial cells. Poonyachoti S and Deachapunya C J. Med. Assoc. Thai. 95 Suppl 12, S105-12, (2012)
Functional analysis and expression of the mono-heme containing cytochrome c subunit of Alternative Complex III in Chloroflexus aurantiacus. Gao X, Majumder EW, Kang Y, et al. Arch. Biochem. Biophys. 535(2), 197-204, (2013)
Generation of reactive oxygen species by a novel berberine-bile acid analog mediates apoptosis in hepatocarcinoma SMMC-7721 cells. Li Q, Zhang L, Zu Y, et al. Biochem. Biophys. Res. Commun. 433(4), 432-7, (2013)
Induction of apoptosis in melanoma A375 cells by a chloroform fraction of Centratherum anthelminticum (L.) seeds involves NF-kappaB, p53 and Bcl-2-controlled mitochondrial signaling pathways. Looi CY, Moharram B, Paydar M, et al. BMC Complement Altern. Med. 13, 166, (2013)
Dynamics of nucleoid structure regulated by mitochondrial fission contributes to cristae reformation and release of cytochrome c. Ban-Ishihara R, Ishihara T, Sasaki N, et al. Proc. Natl. Acad. Sci. U. S. A. 110(29), 11863-8, (2013)
Novel biomarkers of protein oxidation sites and degrees using horse cytochrome c as the target by mass spectrometry Zong, W., et al. Spectrochim. Acta A 78, 1581-1586, (2011)
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